publication . Article . Other literature type . 2014

Truncated and modified amyloid-beta species

Markus Kummer;
Open Access
  • Published: 26 May 2014
  • Publisher: BioMed Central
Abstract
Alzheimer’ s disease pathology is closely connected to the processing of the amyloid precursor protein (APP) resulting in the formation of a variety of amyloid-beta (Aβ ) peptides. They are found as insoluble aggregates in senile plaques, the histopathological hallmark of the disease. These peptides are also found in soluble, mostly monomeric and dimeric, forms in the interstitial and cerebrospinal fluid. Due to the combination of several enzymatic activities during APP processing, Aβ peptides exist in multiple isoforms possessing different N-termini and C-termini. These peptides include, to a certain extent, part of the juxtamembrane and transmembrane domain of...
Subjects
free text keywords: Review, Cognitive Neuroscience, Neurology, Clinical Neurology, Biochemistry, Phosphorylation, Transmembrane domain, Neuroscience, Amyloid beta, biology.protein, biology, Medicine, business.industry, business, Amyloid, Glycosylation, chemistry.chemical_compound, chemistry, Pathology, medicine.medical_specialty, Senile plaques, Gene isoform, Amyloid precursor protein
Funded by
EC| INMIND
Project
INMIND
Imaging of Neuroinflammation in Neurodegenerative Diseases
  • Funder: European Commission (EC)
  • Project Code: 278850
  • Funding stream: FP7 | SP1 | HEALTH
93 references, page 1 of 7

Querfurth, HW, LaFerla, FM. Alzheimer’s disease. N Engl J Med. 2010; 6: 329-344 [PubMed] [DOI]

Mawuenyega, KG, Sigurdson, W, Ovod, V, Munsell, L, Kasten, T, Morris, JC, Yarasheski, KE, Bateman, RJ. Decreased clearance of CNS β-amyloid in Alzheimer’s disease. Science. 2010; 6: 1774-1774 [OpenAIRE] [PubMed] [DOI]

Heneka, MT, O’Banion, MK, Terwel, D, Kummer, MP. Neuroinflammatory processes in Alzheimer’s disease. J Neural Transm Vienna Austria 1996. 2010; 6: 919-947

Thinakaran, G, Koo, EH. Amyloid precursor protein trafficking, processing, and function. J Biol Chem. 2008; 6: 29615-29619 [OpenAIRE] [PubMed] [DOI]

Kuhn, P-H, Wang, H, Dislich, B, Colombo, A, Zeitschel, U, Ellwart, JW, Kremmer, E, Rossner, S, Lichtenthaler, SF. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J. 2010; 6: 3020-3032 [OpenAIRE] [PubMed] [DOI]

Vassar, R, Bennett, BD, Babu-Khan, S, Kahn, S, Mendiaz, EA, Denis, P, Teplow, DB, Ross, S, Amarante, P, Loeloff, R, Luo, Y, Fisher, S, Fuller, J, Edenson, S, Lile, J, Jarosinski, MA, Biere, AL, Curran, E, Burgess, T, Louis, JC, Collins, F, Treanor, J, Rogers, G, Citron, M. Beta-secretase cleavage of Alzheimer’s amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 1999; 6: 735-741 [OpenAIRE] [PubMed] [DOI]

Seubert, P, Vigo-Pelfrey, C, Esch, F, Lee, M, Dovey, H, Davis, D, Sinha, S, Schlossmacher, M, Whaley, J, Swindlehurst, C. Isolation and quantification of soluble Alzheimer’s beta-peptide from biological fluids. Nature. 1992; 6: 325-327 [OpenAIRE] [PubMed] [DOI]

Edbauer, D, Winkler, E, Regula, JT, Pesold, B, Steiner, H, Haass, C. Reconstitution of gamma-secretase activity. Nat Cell Biol. 2003; 6: 486-488 [OpenAIRE] [PubMed] [DOI]

Takami, M, Nagashima, Y, Sano, Y, Ishihara, S, Morishima-Kawashima, M, Funamoto, S, Ihara, Y. γ-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment. J Neurosci Off J Soc Neurosci. 2009; 6: 13042-13052 [DOI]

Qi-Takahara, Y, Morishima-Kawashima, M, Tanimura, Y, Dolios, G, Hirotani, N, Horikoshi, Y, Kametani, F, Maeda, M, Saido, TC, Wang, R, Ihara, Y. Longer forms of amyloid beta protein: implications for the mechanism of intramembrane cleavage by gamma-secretase. J Neurosci Off J Soc Neurosci. 2005; 6: 436-445 [DOI]

Bibl, M, Gallus, M, Welge, V, Lehmann, S, Sparbier, K, Esselmann, H, Wiltfang, J. Characterization of cerebrospinal fluid aminoterminally truncated and oxidized amyloid-β peptides. Proteomics Clin Appl. 2012; 6: 163-169 [OpenAIRE] [PubMed] [DOI]

Haass, C, Selkoe, DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat Rev Mol Cell Biol. 2007; 6: 101-112 [OpenAIRE] [PubMed] [DOI]

Beher, D, Wrigley, JDJ, Owens, AP, Shearman, MS. Generation of C-terminally truncated amyloid-β peptides is dependent on γ-secretase activity. J Neurochem. 2002; 6: 563-575 [OpenAIRE] [PubMed] [DOI]

Portelius, E, Price, E, Brinkmalm, G, Stiteler, M, Olsson, M, Persson, R, Westman-Brinkmalm, A, Zetterberg, H, Simon, AJ, Blennow, K. A novel pathway for amyloid precursor protein processing. Neurobiol Aging. 2011; 6: 1090-1098 [OpenAIRE] [PubMed] [DOI]

Haass, C, Hung, AY, Schlossmacher, MG, Teplow, DB, Selkoe, DJ. β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J Biol Chem. 1993; 6: 3021-3024 [OpenAIRE] [PubMed]

93 references, page 1 of 7
Abstract
Alzheimer’ s disease pathology is closely connected to the processing of the amyloid precursor protein (APP) resulting in the formation of a variety of amyloid-beta (Aβ ) peptides. They are found as insoluble aggregates in senile plaques, the histopathological hallmark of the disease. These peptides are also found in soluble, mostly monomeric and dimeric, forms in the interstitial and cerebrospinal fluid. Due to the combination of several enzymatic activities during APP processing, Aβ peptides exist in multiple isoforms possessing different N-termini and C-termini. These peptides include, to a certain extent, part of the juxtamembrane and transmembrane domain of...
Subjects
free text keywords: Review, Cognitive Neuroscience, Neurology, Clinical Neurology, Biochemistry, Phosphorylation, Transmembrane domain, Neuroscience, Amyloid beta, biology.protein, biology, Medicine, business.industry, business, Amyloid, Glycosylation, chemistry.chemical_compound, chemistry, Pathology, medicine.medical_specialty, Senile plaques, Gene isoform, Amyloid precursor protein
Funded by
EC| INMIND
Project
INMIND
Imaging of Neuroinflammation in Neurodegenerative Diseases
  • Funder: European Commission (EC)
  • Project Code: 278850
  • Funding stream: FP7 | SP1 | HEALTH
93 references, page 1 of 7

Querfurth, HW, LaFerla, FM. Alzheimer’s disease. N Engl J Med. 2010; 6: 329-344 [PubMed] [DOI]

Mawuenyega, KG, Sigurdson, W, Ovod, V, Munsell, L, Kasten, T, Morris, JC, Yarasheski, KE, Bateman, RJ. Decreased clearance of CNS β-amyloid in Alzheimer’s disease. Science. 2010; 6: 1774-1774 [OpenAIRE] [PubMed] [DOI]

Heneka, MT, O’Banion, MK, Terwel, D, Kummer, MP. Neuroinflammatory processes in Alzheimer’s disease. J Neural Transm Vienna Austria 1996. 2010; 6: 919-947

Thinakaran, G, Koo, EH. Amyloid precursor protein trafficking, processing, and function. J Biol Chem. 2008; 6: 29615-29619 [OpenAIRE] [PubMed] [DOI]

Kuhn, P-H, Wang, H, Dislich, B, Colombo, A, Zeitschel, U, Ellwart, JW, Kremmer, E, Rossner, S, Lichtenthaler, SF. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J. 2010; 6: 3020-3032 [OpenAIRE] [PubMed] [DOI]

Vassar, R, Bennett, BD, Babu-Khan, S, Kahn, S, Mendiaz, EA, Denis, P, Teplow, DB, Ross, S, Amarante, P, Loeloff, R, Luo, Y, Fisher, S, Fuller, J, Edenson, S, Lile, J, Jarosinski, MA, Biere, AL, Curran, E, Burgess, T, Louis, JC, Collins, F, Treanor, J, Rogers, G, Citron, M. Beta-secretase cleavage of Alzheimer’s amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 1999; 6: 735-741 [OpenAIRE] [PubMed] [DOI]

Seubert, P, Vigo-Pelfrey, C, Esch, F, Lee, M, Dovey, H, Davis, D, Sinha, S, Schlossmacher, M, Whaley, J, Swindlehurst, C. Isolation and quantification of soluble Alzheimer’s beta-peptide from biological fluids. Nature. 1992; 6: 325-327 [OpenAIRE] [PubMed] [DOI]

Edbauer, D, Winkler, E, Regula, JT, Pesold, B, Steiner, H, Haass, C. Reconstitution of gamma-secretase activity. Nat Cell Biol. 2003; 6: 486-488 [OpenAIRE] [PubMed] [DOI]

Takami, M, Nagashima, Y, Sano, Y, Ishihara, S, Morishima-Kawashima, M, Funamoto, S, Ihara, Y. γ-Secretase: successive tripeptide and tetrapeptide release from the transmembrane domain of beta-carboxyl terminal fragment. J Neurosci Off J Soc Neurosci. 2009; 6: 13042-13052 [DOI]

Qi-Takahara, Y, Morishima-Kawashima, M, Tanimura, Y, Dolios, G, Hirotani, N, Horikoshi, Y, Kametani, F, Maeda, M, Saido, TC, Wang, R, Ihara, Y. Longer forms of amyloid beta protein: implications for the mechanism of intramembrane cleavage by gamma-secretase. J Neurosci Off J Soc Neurosci. 2005; 6: 436-445 [DOI]

Bibl, M, Gallus, M, Welge, V, Lehmann, S, Sparbier, K, Esselmann, H, Wiltfang, J. Characterization of cerebrospinal fluid aminoterminally truncated and oxidized amyloid-β peptides. Proteomics Clin Appl. 2012; 6: 163-169 [OpenAIRE] [PubMed] [DOI]

Haass, C, Selkoe, DJ. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat Rev Mol Cell Biol. 2007; 6: 101-112 [OpenAIRE] [PubMed] [DOI]

Beher, D, Wrigley, JDJ, Owens, AP, Shearman, MS. Generation of C-terminally truncated amyloid-β peptides is dependent on γ-secretase activity. J Neurochem. 2002; 6: 563-575 [OpenAIRE] [PubMed] [DOI]

Portelius, E, Price, E, Brinkmalm, G, Stiteler, M, Olsson, M, Persson, R, Westman-Brinkmalm, A, Zetterberg, H, Simon, AJ, Blennow, K. A novel pathway for amyloid precursor protein processing. Neurobiol Aging. 2011; 6: 1090-1098 [OpenAIRE] [PubMed] [DOI]

Haass, C, Hung, AY, Schlossmacher, MG, Teplow, DB, Selkoe, DJ. β-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J Biol Chem. 1993; 6: 3021-3024 [OpenAIRE] [PubMed]

93 references, page 1 of 7
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publication . Article . Other literature type . 2014

Truncated and modified amyloid-beta species

Markus Kummer;